Closed State of Gramicidin Channel Detected by X-Ray Inplane Scattering

by He, K.; Ludtke, S. J.; Wu, Yanqi; Huang, Huey W.; Andersen, Olaf S.; Greathouse, Denise V.; Koeppe II, R. Erdman

An analogue of gramicidin A (gA) was synthesized with the formyl group replaced by a BOC group. The analogue (BOC-gA) exhibited single channel conduction, but the channel is 5-order-of-magnitude destabilized relative to the gA channel. Hydrated mixtures of gramicidin and dilauroyl phosphatidylcholine in the molar ratio of 1:10 were prepared into uniformly aligned multiple bilayers, and X-ray scattering with the momentum transfer in the plane of the membrane was measured. Analysis with the help of computer simulations showed that 70% of BOC-gA are monomers. Thus for the first time it was shown that gramicidin monomers are stable inside the monolayers of a lipid membrane. Furthermore, the monomers have the same beta helical conformation as the dimeric channel. The result suggests the possibility that when a gramicidin channel is closed, it dissociates into two monomers floating in opposite monolayers.

Journal
Biophysical Chemistry
Volume
49
Issue
1
Year
1994
Start Page
83
ISBN/ISSN
1873-4200; 0301-4622
DOI
10.1016/0301-4622(93)E0085-J